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Protein

Carbon monoxide dehydrogenase

Gene

cooS

Organism
Rhodospirillum rubrum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).By similarity

Catalytic activityi

CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi41Iron-sulfur 1 (4Fe-4S); shared with dimeric partner1 Publication1
Metal bindingi49Iron-sulfur 1 (4Fe-4S); shared with dimeric partner1 Publication1
Metal bindingi50Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi53Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi58Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi72Iron-sulfur 2 (4Fe-4S)1 Publication1
Metal bindingi265Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogen1 Publication1
Metal bindingi300Nickel-iron-sulfur (Ni-4Fe-4S)1 Publication1
Metal bindingi338Nickel-iron-sulfur (Ni-4Fe-4S)1 Publication1
Metal bindingi451Nickel-iron-sulfur (Ni-4Fe-4S)1 Publication1
Metal bindingi481Nickel-iron-sulfur (Ni-4Fe-4S)1 Publication1
Metal bindingi531Nickel-iron-sulfur (Ni-4Fe-4S)1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Nickel

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16431.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase (EC:1.2.7.4By similarity)
Short name:
CODH
Gene namesi
Name:cooS
OrganismiRhodospirillum rubrum
Taxonomic identifieri1085 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi265H → V: Great decrease in activity; diminishes incorporation of nickel. Displays hydroxylamine reductase activity. 1 Publication1
Mutagenesisi531C → A: Displays hydrogenase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001571392 – 639Carbon monoxide dehydrogenaseAdd BLAST638

Expressioni

Inductioni

By carbon monoxide; under anaerobic conditions.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi269796.Rru_A1427.

Structurei

Secondary structure

1639
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 37Combined sources8
Helixi42 – 46Combined sources5
Beta strandi62 – 66Combined sources5
Helixi76 – 109Combined sources34
Turni110 – 112Combined sources3
Helixi122 – 131Combined sources10
Turni137 – 139Combined sources3
Helixi141 – 154Combined sources14
Turni155 – 157Combined sources3
Helixi166 – 171Combined sources6
Helixi174 – 183Combined sources10
Helixi190 – 200Combined sources11
Helixi209 – 238Combined sources30
Beta strandi244 – 250Combined sources7
Beta strandi257 – 265Combined sources9
Helixi267 – 279Combined sources13
Turni280 – 282Combined sources3
Helixi283 – 286Combined sources4
Beta strandi292 – 298Combined sources7
Helixi299 – 308Combined sources10
Beta strandi313 – 315Combined sources3
Turni318 – 321Combined sources4
Helixi322 – 325Combined sources4
Beta strandi331 – 334Combined sources4
Beta strandi336 – 338Combined sources3
Helixi343 – 348Combined sources6
Beta strandi353 – 356Combined sources4
Beta strandi366 – 368Combined sources3
Helixi373 – 375Combined sources3
Helixi376 – 391Combined sources16
Beta strandi406 – 410Combined sources5
Helixi414 – 422Combined sources9
Helixi430 – 439Combined sources10
Beta strandi440 – 442Combined sources3
Beta strandi444 – 448Combined sources5
Helixi460 – 471Combined sources12
Beta strandi474 – 479Combined sources6
Helixi480 – 489Combined sources10
Helixi494 – 500Combined sources7
Helixi503 – 515Combined sources13
Beta strandi518 – 520Combined sources3
Beta strandi524 – 531Combined sources8
Helixi534 – 547Combined sources14
Turni552 – 554Combined sources3
Beta strandi555 – 561Combined sources7
Helixi567 – 579Combined sources13
Beta strandi582 – 587Combined sources6
Turni590 – 593Combined sources4
Helixi595 – 602Combined sources8
Helixi604 – 608Combined sources5
Beta strandi612 – 615Combined sources4
Helixi619 – 635Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQKX-ray2.80A/B/C/D/E/F1-639[»]
DisProtiDP00239.
ProteinModelPortaliP31896.
SMRiP31896.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31896.

Family & Domainsi

Domaini

Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CJG. Bacteria.
COG1151. LUCA.

Family and domain databases

Gene3Di1.20.1270.30. 1 hit.
3.40.50.2030. 2 hits.
InterProiIPR016101. CO_DH_a-bundle.
IPR010047. CODH.
IPR004137. HCP/CODH.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF005023. CODH. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01702. CO_DH_cata. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHHDCAHCS SDACATEMLN LAEANSIETA WHRYEKQQPQ CGFGSAGLCC
60 70 80 90 100
RICLKGPCRI DPFGEGPKYG VCGADRDTIV ARHLVRMIAA GTAAHSEHGR
110 120 130 140 150
HIALAMQHIS QGELHDYSIR DEAKLYAIAK TLGVATEGRG LLAIVGDLAA
160 170 180 190 200
ITLGDFQNQD YDKPCAWLAA SLTPRRVKRL GDLGLLPHNI DASVAQTMSR
210 220 230 240 250
THVGCDADPT NLILGGLRVA MADLDGSMLA TELSDALFGT PQPVVSAANL
260 270 280 290 300
GVMKRGAVNI AVNGHNPMLS DIICDVAADL RDEAIAAGAA EGINIIGICC
310 320 330 340 350
TGHEVMMRHG VPLATNYLSQ ELPILTGALE AMVVDVQCIM PSLPRIAECF
360 370 380 390 400
HTQIITTDKH NKISGATHVP FDEHKAVETA KTIIRMAIAA FGRRDPNRVA
410 420 430 440 450
IPAFKQKSIV GFSAEAVVAA LAKVNADDPL KPLVDNVVNG NIQGIVLFVG
460 470 480 490 500
CNTTKVQQDS AYVDLAKSLA KRNVLVLATG CAAGAFAKAG LMTSEATTQY
510 520 530 540 550
AGEGLKGVLS AIGTAAGLGG PLPLVMHMGS CVDNSRAVAL ATALANKLGV
560 570 580 590 600
DLSDLPLVAS APECMSEKAL AIGSWAVTIG LPTHVGSVPP VIGSQIVTKL
610 620 630
VTETAKDLVG GYFIVDTDPK SAGDKLYAAI QERRAGLGL
Length:639
Mass (Da):66,854
Last modified:July 1, 1993 - v1
Checksum:iDCADD7C13D8D85B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65510 Genomic DNA. Translation: AAC45123.1.
PIRiC42957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65510 Genomic DNA. Translation: AAC45123.1.
PIRiC42957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQKX-ray2.80A/B/C/D/E/F1-639[»]
DisProtiDP00239.
ProteinModelPortaliP31896.
SMRiP31896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A1427.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CJG. Bacteria.
COG1151. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16431.

Miscellaneous databases

EvolutionaryTraceiP31896.

Family and domain databases

Gene3Di1.20.1270.30. 1 hit.
3.40.50.2030. 2 hits.
InterProiIPR016101. CO_DH_a-bundle.
IPR010047. CODH.
IPR004137. HCP/CODH.
IPR011254. Prismane-like.
IPR016099. Prismane-like_a/b-sand.
[Graphical view]
PfamiPF03063. Prismane. 1 hit.
[Graphical view]
PIRSFiPIRSF005023. CODH. 1 hit.
SUPFAMiSSF56821. SSF56821. 1 hit.
TIGRFAMsiTIGR01702. CO_DH_cata. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCOOS_RHORU
AccessioniPrimary (citable) accession number: P31896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Methyl viologen can act as acceptor. Inactivated by O2.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.